Recombinant Human EphA8 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EphA8 Fc Chimera is coated at 2 μg/mL (100 μL/well), the concentration of Biotinylayed Recombinant Human Ephrin-A5 Fc Chimera (Catalog # BT374) that produces 50% of the optimal binding response is 2-12 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EphA8 protein
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
83.2 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
94 kDa, reducing conditions
Publications
Read Publication using 6828-A8 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after opening.
3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, PEG, CHAPS and Imidazole.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human EphA8 Fc Chimera Protein, CF
Eek
EK3
EPH- and ELK-related kinase
EPH- and ELK-related tyrosine kinase
EPH receptor A8
EphA8
EPH-like kinase 3
ephrin type-A receptor 8
Hek3
hydroxyaryl-protein kinase
KIAA1459
protein-tyrosine kinase
tyrosine-protein kinase receptor EEK
tyrosylprotein kinase
Background
EphA8, also known as Hek3 and Eek, is a 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases (1, 2). The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. EphA4 binds and is activated by class A Ephrins but not class B Ephrins (3, 4). Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. The 512 amino acid (aa) extracellular domain (ECD) of human EphA8 contains an N-terminal Ephrin binding region, a cysteine-rich region, and two fibronectin type III domains (FnIII). The 442 aa cytoplasmic domain contains the tyrosine kinase domain and a sterile alpha motif (SAM) (5). Within the ECD, human EphA8 shares 97% aa sequence identity with mouse and rat EphA8. EphA8 is expressed in neurons in the mesencephalon of the developing brain, particularly in the rostral tectum and the superior colliculus (6-8). It is enriched at the tips of neurite processes and plays a role in projection of superior colliculus axons through the posterior commissure (7, 9). Its expression enhances neurite extension by means of a mechanism that does not require catalytic activity of the tyrosine kinase domain (10). Ephrin-mediated activation of the EphA8 kinase induces phosphorylation of tyrosine residues in the cytoplasmic domain, leading to association with signaling and scaffolding proteins and inhibition of cell-cell adhesion (4, 9, 11). Ligand binding can also promote the Integrin-mediated cellular adhesion to Fibronectin (12). This function, like the enhancement of neurite extension, does not require activation of the kinase domain (12).
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